The RecA protein of Helicobacter pylori requires a posttranslational modification for full activity
The RecA protein of Helicobacter pylori requires a posttranslational modification for full activity
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DOI：
10.1128/jb.186.3.777-784.2004
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发表时间：
2004-02-01
影响因子：
3.2
通讯作者：
Haas, R
中科院分区：
文献类型：
--
作者：
Fischer, W;Haas, R
在大多数细菌中，RecA蛋白是同源重组机制和SOS系统的中心组成部分。在执行这些功能的过程中，它参与了DNA修复过程，并在自然转化能力中发挥着重要作用。这在幽门螺杆菌中可能特别重要，在幽门螺杆菌中，菌株之间通过同源重组产生了异常高度的微多样性。我们以前已经提出，H.Pylori RecA蛋白受到翻译后修饰的影响，导致其凝胶迁移率略有变化。在这里，我们证明了至少有两个recA下游的基因参与了这一修饰，并且这一过程依赖于参与糖基化和脂多糖生物合成的基因。一个假定的糖基化位点的定点突变导致了生产。一种未经修饰的RecA蛋白。这种翻译后修饰不涉及膜靶向或细胞分裂功能，但对于RecA在DNA修复中的全部功能是必要的。因此，它可能是对幽门螺杆菌在其自然环境中的特定要求的适应。
The RecA protein is a central component of the homologous recombination machinery and of the SOS system in most bacteria. In performing these functions, it is involved in DNA repair processes and plays an important role in natural transformation competence. This may be especially important in Helicobacter pylori, where an unusually high degree of microdiversity among strains is generated by homologous recombination. We have suggested previously that the H. pylori RecA protein is subject to posttranslational modifications that result in a slight shift in its electrophoretic mobility. Here we show that at least two genes downstream of recA are involved in this modification and that this process is dependent on genes involved in glycosylation and lipopolysaccharide biosynthesis. Site-directed mutagenesis of a putative glycosylation site results in production. of an unmodified RecA protein. This posttranslational modification is not involved in membrane targeting or cell division functions but is necessary for the full function of RecA in DNA repair. Thus, it might be an adaptation to the specific requirements of H. pylori in its natural environment.